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Noncovalent dimerization of ubiquitin.

ABSTRACT: Another kind of dynamics: Ubiquitin noncovalently dimerizes with a dissociation constant of approximately 5?mM. The two subunits adopt an array of relative orientations, utilizing an interface also for binding to other proteins (see picture). Quaternary fluctuation among members of the dimer ensemble constitutes a different kind of dynamics that complements the tertiary dynamics of each ubiquitin subunit.

SUBMITTER: Liu Z

PROVIDER: S-EPMC3303887 | biostudies-other | 2012 Jan

REPOSITORIES: biostudies-other

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Noncovalent dimerization of ubiquitin.

Liu Zhu Z Zhang Wei-Ping WP Xing Qiong Q Ren Xuefeng X Liu Maili M Tang Chun C

Angewandte Chemie (International ed. in English) 20111123 2

Another kind of dynamics: Ubiquitin noncovalently dimerizes with a dissociation constant of approximately 5 mM. The two subunits adopt an array of relative orientations, utilizing an interface also for binding to other proteins (see picture). Quaternary fluctuation among members of the dimer ensemble constitutes a different kind of dynamics that complements the tertiary dynamics of each ubiquitin subunit. ...[more]

PMID: 22109817

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